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- W2080976162 abstract "Abstract A nucleic acid bound poly(A) polymerase has been purified (2400-fold) from mung bean hypocotyls by employing polymin-P, ATP-Sepharose affinity matrix and DE-52 ion-exchange chromatography. The purified enzyme is free of nucleases and RNA polymerase II activities. The enzyme was purified to electrophoretic homogeneity as confirmed by the presence of a single silver stained band on native PAG. The molecular weight of poly(A) polymerase is 120 000 as determined by gel permeation on Sephacryl S-200. Fractionation of purified enzyme on SDS-PAG revealed a single silver stained band. The molecular weight of the enzyme subunit on denaturing gels was 30 000. This indicated the oligomeric nature of poly(A) polymerase. The pH optimum of the purified enzyme is 8.0 and requires Mn2+ (2mM), dithiothreitol (5mM) and primer RNA for its optimum activity at 37°C. Both poly(A) and wheat embryo RNA served as efficient primers for enzyme catalyzed reaction. The Km of enzyme for ATP is 47 μM. The purified enzyme exhibited an initial lag of 30 min, but thereafter the enzyme activity increased linearly up to 120 min. This lag phase could not be abolished even at high concentration of the purified enzyme. The enzyme activity is proportional to the protein concentration in the range of 0.1–0.4 μg. The 3H-labelled reaction product binds to poly(U) Sephadex affinity matrix and is insensitive to the nucleolytic action of RNase A and RNase T1. This proved the polyadenylate nature of the reaction product." @default.
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- W2080976162 date "1989-01-01" @default.
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- W2080976162 title "Purification of poly (A) polymerase from mung bean hypocotyls: Subunit structure, molecular properties and characterization of the reaction product" @default.
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- W2080976162 doi "https://doi.org/10.1016/0168-9452(89)90040-x" @default.
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